Solution NMR structure of the coldâshock protein from the hyperthermophilic bacterium Thermotoga maritima
2001
Kremer, Werner | Schuler, Benjamin | Harrieder, Stefan | Geyer, Matthias | Gronwald, Wolfram | Welker, Christine | Jaenicke, Rainer | Kalbitzer, Hans R.
Coldâshock proteins (Csps) are a subgroup of the coldâinduced proteins preferentially expressed in bacteria and other organisms on reduction of the growth temperature below the physiological temperature. They are related to the coldâshock domain found in eukaryotes and are some of the most conserved proteins known. Their exact function is still not known, but translational regulation, possibly via RNA chaperoning, has been discussed.âHere we present the structure of a hyperthermophilic member of the Csp family. The NMR solution structure of TmCsp from Thermotoga maritima, the hyperthermophilic member of this class of proteins, was solved on the basis of 1015 conformational constraints. It contains five β strands combined in two antiparallel β sheets making up a β barrel structure, in which β strands 1–4 are arranged in a Greekâkey topology. The side chain of R2, which is exclusively found in thermophilic members of the Csp family, probably participates in a peripheral ion cluster involving residues D20, R2, E47 and K63, suggesting that the thermostability of TmCsp is based on the peripheral ion cluster around the side chain of R2.
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